STRESTMARQ/抗HSP27抗体（pSer15）/SPC-1263D-BI/100-µl-免疫在线蚂蚁淘旗下平台

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STRESTMARQ/抗HSP27抗体（pSer15）/SPC-1263D-BI/100-µl

商品编号： SPC-1263D-BI

品牌： StressMarq Biosciences

市场价： ¥5960.00

美元价： 3576.00

产地：美国(厂家直采)

公司：

产品分类：酸碱缓冲液

公司分类： acid_base_buffer_solution

联系Q Q： 3392242852

电话号码： 4000-520-616

电子邮箱： info@ebiomall.com

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商品介绍

Overview:

Product Name HSP27 Antibody (pSer15)

Description

Rabbit Anti-Human HSP27 (pSer15) Polyclonal

Species Reactivity Human, Mouse, Rat

Applications WB, IHC, ICC/IF

Antibody Dilution WB (1:1000), IHC (1:100), ICC/IF (1:200); optimal dilutions for assays should be determined by the user.

Host Species Rabbit

Immunogen Species Human

Immunogen Synthesized phosphopeptide derived from human HSP27 around the phosphorylation site of serine15 (G-P-SP-W-D).

Conjugates

Alkaline Phosphatase, APC, ATTO 390, ATTO 488, ATTO 565, ATTO 594, ATTO 633, ATTO 655, ATTO 680, ATTO 700, Biotin, FITC, HRP, PE/ATTO 594, PerCP, RPE, Streptavidin, Unconjugated

Properties

Storage Buffer	PBS pH 7.4, 50% glycerol, 150mM NaCl, 0.02% sodium azide
Storage Temperature	-20ºC
Shipping Temperature	Blue Ice or 4ºC
Purification	Affinity Purified
Clonality	Polyclonal
Isotype	IgG
Specificity	Detects endogenous levels of HSP27only when phosphorylated at serine 15.
Cite This Product	StressMarq Biosciences Cat# SPC-1263, RRID: AB_2712539
Certificate of Analysis	A 1:1000 dilution of SPC-1263 was sufficient for detection of Hsp27 in 10 µg of HeLa cell lysates by ECL immunoblot analysis using Goat Anti-Rabbit IgG:HRP as the secondary antibody.

Biological Description

Alternative Names	28kDa heat shock protein Antibody, CMT2F Antibody, HSP25 Antibody, HSP27 Antibody, HSP28 Antibody, HSPB1 Antibody, SRP27 Antibody
Research Areas	Cancer, Heat Shock, Atherosclerosis, Cardiovascular System, Chaperone Proteins, Chaperones, Heart, Protein Trafficking, Trafficking
Cellular Localization	Cytoplasm, Nucleus
Accession Number	NP_001531.1
Gene ID	3315
Swiss Prot	P04792
Scientific Background	HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an α-crystallin domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
References	1. Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599. 2. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56. 3. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229. 4. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70. 5. Sarto C., Binnz P.A., and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26. 6. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.

Product Images

<p>Immunohistochemistry analysis using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263). Tissue: Breast Carcinoma Tissue. Species: Human. Fixation: Formalin fixed paraffin-embedded. Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263) at 1:1000. The image on the right is treated with the synthesized peptide.</p>

Immunohistochemistry analysis using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263). Tissue: Breast Carcinoma Tissue. Species: Human. Fixation: Formalin fixed paraffin-embedded. Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263) at 1:1000. The image on the right is treated with the synthesized peptide.

<p>Western blot analysis of Human HeLa cell lysates showing detection of ~27kDa Hsp27 protein using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263). Lane 1 and Lane 2: Human HeLa, Hsp27 Antibody (Ser15). Lane 3 and Lane 4: Human HeLa, Hsp27 Antibody (pSer15). Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263) at 1:1000. Predicted/Observed Size: ~27kDa.</p>

Western blot analysis of Human HeLa cell lysates showing detection of ~27kDa Hsp27 protein using Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263). Lane 1 and Lane 2: Human HeLa, Hsp27 Antibody (Ser15). Lane 3 and Lane 4: Human HeLa, Hsp27 Antibody (pSer15). Primary Antibody: Rabbit Anti-Hsp27 Polyclonal Antibody (SPC-1263) at 1:1000. Predicted/Observed Size: ~27kDa.

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Biotin

Properties:

Binds tetrameric avidin proteins including Streptavidin and neuravidin with very high affinity
Molar mass: 244.31 g/mol
Formula: C₁₀H₁₆N₂O₃S
Applications: Western blot, immunohistochemistry, and ELISA

Biotin Datasheet

品牌介绍

StressMarq Biosciences公司的核心技术领域为细胞应激与离子通道以及载体研究，同时在其他领域也取得了一定成就，包括翻译后修饰，提供甲基化与乙酰基化抗体。其中，细胞应激领域主要包括热休克蛋白（HSP）领域。我们公司不仅在热休克蛋白领域领先全球，而且在氧化应激领域也卓有成就。StressMarq的优势在于提供四种独立的产品系列，分别涉及抗体、蛋白、酶联免疫吸附试验（ELISA）试剂盒及小分子领域。

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